| RRC ID |
39527
|
| Author |
Yokota S, Kayano T, Ohta T, Kurimoto M, Yanagi H, Yura T, Kubota H.
|
| Title |
Proteasome-dependent degradation of cytosolic chaperonin CCT.
|
| Journal |
Biochem Biophys Res Commun
|
| Abstract |
The chaperonin containing t-complex polypeptide 1 (CCT) is a heterooligomeric molecular chaperone that assists in the folding of actin, tubulin, and other cytosolic proteins. We show here that degradation of CCT in mammalian cells is inhibited by a proteasome-specific inhibitor, lactacystin. When CCT synthesis was inhibited by growth arrest of cells, the decrease in CCT levels was much slower in the presence of lactacystin than in its absence. Pulse-chase experiments indicated that degradation of CCT is inhibited 2- to 2.5-fold by addition of lactacystin. In addition, CCT degradation rate in ts85 cells that produce thermolabile ubiquitin-activating enzyme E1 was reduced 3-fold at the nonpermissive temperature compared to the degradation at the permissive temperature. These results indicate that the ubiquitin-proteasome system is involved in CCT degradation.
|
| Volume |
279(2)
|
| Pages |
712-7
|
| Published |
2000-12-20
|
| DOI |
10.1006/bbrc.2000.4011
|
| PII |
S0006291X00940117
|
| PMID |
11118350
|
| MeSH |
Acetylcysteine / analogs & derivatives*
Acetylcysteine / pharmacology
Adenosine Triphosphatases / metabolism
Animals
Cell Division
Chaperonin Containing TCP-1
Chaperonins / metabolism*
Cysteine Endopeptidases / metabolism*
Cysteine Proteinase Inhibitors / pharmacology
Cytosol / metabolism
Enzyme Stability
Female
Kinetics
Ligases / metabolism
Mammary Neoplasms, Experimental
Mice
Multienzyme Complexes / metabolism*
Multiple Myeloma
Protease Inhibitors / pharmacology
Proteasome Endopeptidase Complex
Temperature
Thermodynamics
Tumor Cells, Cultured
Ubiquitin-Activating Enzymes
Ubiquitin-Protein Ligases
|
| IF |
2.985
|
| Times Cited |
12
|
|
WOS Category
|
BIOPHYSICS
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
| Resource |
| Human and Animal Cells |
DA-3(RCB1144)
WEHI-3(RCB0035)
FM3A(RCB0086) |
